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PDBsum entry 3pco

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protein ligands Protein-protein interface(s) links
Ligase PDB id
3pco
Jmol PyMol
Contents
Protein chains
242 a.a. *
795 a.a. *
323 a.a. *
Ligands
PHE ×2
AMP ×2
* Residue conservation analysis
PDB id:
3pco
Name: Ligase
Title: Crystal structure of e. Coli phenylalanine-tRNA synthetasE C with phenylalanine and amp
Structure: Phenylalanyl-tRNA synthetase, alpha subunit. Chain: a, c. Fragment: ligase. Engineered: yes. Phenylalanyl-tRNA synthetase, beta chain. Chain: b, d. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: ecdh1_1928. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
3.02Å     R-factor:   0.235     R-free:   0.300
Authors: I.Mermershtain,I.Finarov,L.Klipcan,N.Kessler,H.Rozenberg,M.G
Key ref: I.Mermershtain et al. (2011). Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP. Protein Sci, 20, 160-167. PubMed id: 21082706
Date:
21-Oct-10     Release date:   02-Mar-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
C9QTZ3  (C9QTZ3_ECOD1) -  Phenylalanyl-tRNA synthetase subunit alpha
Seq:
Struc:
327 a.a.
242 a.a.
Protein chains
Pfam   ArchSchema ?
P07395  (SYFB_ECOLI) -  Phenylalanine--tRNA ligase beta subunit
Seq:
Struc:
 
Seq:
Struc:
795 a.a.
795 a.a.
Protein chain
Pfam   ArchSchema ?
C9QTZ3  (C9QTZ3_ECOD1) -  Phenylalanyl-tRNA synthetase subunit alpha
Seq:
Struc:
327 a.a.
323 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.6.1.1.20  - Phenylalanine--tRNA ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe)
ATP
+
L-phenylalanine
Bound ligand (Het Group name = PHE)
corresponds exactly
+ tRNA(Phe)
=
AMP
Bound ligand (Het Group name = AMP)
corresponds exactly
+ diphosphate
+ L-phenylalanyl- tRNA(Phe)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   4 terms 
  Biological process     translation   4 terms 
  Biochemical function     nucleotide binding     11 terms  

 

 
    reference    
 
 
Protein Sci 20:160-167 (2011)
PubMed id: 21082706  
 
 
Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP.
I.Mermershtain, I.Finarov, L.Klipcan, N.Kessler, H.Rozenberg, M.G.Safro.
 
  ABSTRACT  
 
No abstract given.

 

 

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